Proton-coupled dynamics in lactose permease.

@article{Andersson2012ProtoncoupledDI,
  title={Proton-coupled dynamics in lactose permease.},
  author={Magnus Andersson and Ana-Nicoleta Bondar and J. Alfredo Freites and Douglas J. Tobias and H Ronald Kaback and Stephen H White},
  journal={Structure},
  year={2012},
  volume={20 11},
  pages={1893-904}
}
Lactose permease of Escherichia coli (LacY) catalyzes symport of a galactopyranoside and an H⁺ via an alternating access mechanism. The transition from an inward- to an outward-facing conformation of LacY involves sugar-release followed by deprotonation. Because the transition depends intimately upon the dynamics of LacY in a bilayer environment, molecular dynamics (MD) simulations may be the only means of following the accompanying structural changes in atomic detail. Here, we describe MD… CONTINUE READING
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